LPXN

From Wikipedia, the free encyclopedia

Leupaxin

PDB rendering based on 1x3h.

Available structures: 1x3h

Identifiers

Symbol(s)

LPXN; LDPL

External IDs

OMIM: 605390 MGI: 2147677 HomoloGene: 3536

Gene ontology
Molecular Function:	• zinc ion binding • metal ion binding
Cellular Component:	• cytoplasm
Biological Process:	• protein complex assembly • cell adhesion • signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004811 (mRNA)
NP_004802 (protein)

NM_134152 (mRNA)
NP_598913 (protein)

Location

Chr 11: 58.05 - 58.1 Mb

Chr 19: 12.86 - 12.9 Mb

Pubmed search

[1]

[2]

Leupaxin, also known as LPXN, is a human gene.^[1]

The product encoded by this gene is preferentially expressed in hematopoietic cells and is most homologous to the focal adhesion protein, paxillin. It may function in cell type-specific signaling by associating with PYK2, a member of focal adhesion kinase family. As a substrate for a tyrosine kinase in lymphoid cells, this protein may also function in, and be regulated by tyrosine kinase activity.^[1]

[edit] References

^ ^a ^b Entrez Gene: LPXN leupaxin.

[edit] Further reading

Chew V, Lam KP (2007). "Leupaxin negatively regulates B cell receptor signaling.". J. Biol. Chem. 282 (37): 27181–91. doi:10.1074/jbc.M704625200. PMID 17640867.
Sahu SN, Nunez S, Bai G, Gupta A (2007). "Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells.". Am. J. Physiol., Cell Physiol. 292 (6): C2288–96. doi:10.1152/ajpcell.00503.2006. PMID 17329398.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Tao WA, Wollscheid B, O'Brien R, et al. (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry.". Nat. Methods 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384.
Watanabe N, Amano N, Ishizuka H, Mashima K (2005). "Leupaxin binds to PEST domain tyrosine phosphatase PEP.". Mol. Cell. Biochem. 269 (1-2): 13–7. PMID 15786712.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
Gupta A, Lee BS, Khadeer MA, et al. (2003). "Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast.". J. Bone Miner. Res. 18 (4): 669–85. PMID 12674328.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Liu S, Thomas SM, Woodside DG, et al. (2000). "Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses.". Nature 402 (6762): 676–81. doi:10.1038/45264. PMID 10604475.
Lipsky BP, Beals CR, Staunton DE (1998). "Leupaxin is a novel LIM domain protein that forms a complex with PYK2.". J. Biol. Chem. 273 (19): 11709–13. PMID 9565592.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.